PMID: 6406483May 25, 1983Paper

Modulation of the number of ligand binding sites of UDP-glucuronyltransferase by the gel to liquid-crystal phase transition of phosphatidylcholines.

The Journal of Biological Chemistry
Y HochmanD Zakim

Abstract

The kinetics of a pure, delipidated form of microsomal UDP-glucuronyltransferase is non-Michaelis-Menten when the enzyme is reconstituted into unilamellar vesicles of phosphatidylcholine that are in a gel phase. Double reciprocal plots of velocity as a function of the concentration of UDP-glucuronic acid show a downward curvature under these conditions. Binding studies indicate that the basis for the kinetic pattern is the presence of one high affinity and one low affinity binding site for UDP-glucuronic acid. The two classes of binding sites seem to be generated by the presence of two subunits that bind UDP-glucuronic acid within a single molecule of UDP-glucuronyltransferase. Melting the phospholipids from the gel phase to the liquid-crystal phase is associated with a switch from non-Michaelis-Menten to Michaelis-Menten kinetics for UDP-glucuronyltransferase. Binding studies for interaction of UDP-glucuronic acid with enzyme present in a liquid-crystal lipid phase indicate that the two binding sites for UDP-glucuronic acid do not become identical in this setting. Instead, one of the sites becomes nonfunctional. Binding studies carried out with UDP as ligand lead to similar results. There is a high affinity and a low affinity ...Continue Reading

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